TM1R_SOLLC
ID TM1R_SOLLC Reviewed; 754 AA.
AC A7M6E7;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=ToMV resistance protein Tm-1(GCR237) {ECO:0000303|PubMed:17699618};
DE AltName: Full=Disease resistance protein Tm-1 {ECO:0000305};
DE AltName: Full=Protein p80(GCR237) {ECO:0000303|PubMed:17699618};
GN Name=Tm-1 {ECO:0000303|PubMed:17699618};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION
RP WITH TOMATO MOSAIC VIRUS REPLICATION PROTEINS (MICROBIAL INFECTION).
RC STRAIN=cv. Craigella GCR237;
RX PubMed=17699618; DOI=10.1073/pnas.0703203104;
RA Ishibashi K., Masuda K., Naito S., Meshi T., Ishikawa M.;
RT "An inhibitor of viral RNA replication is encoded by a plant resistance
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13833-13838(2007).
RN [2]
RP FUNCTION.
RX PubMed=3686829; DOI=10.1016/0042-6822(87)90147-4;
RA Watanabe Y., Kishibayashi N., Motoyoshi F., Okada Y.;
RT "Characterization of Tm-1 gene action on replication of common isolates and
RT a resistance-breaking isolate of TMV.";
RL Virology 161:527-532(1987).
RN [3]
RP GENE FAMILY.
RX PubMed=24710868; DOI=10.1007/s001220050745;
RA Ohmori T., Murata M., Motoyoshi F.;
RT "Characterization of disease resistance gene-like sequences in near-
RT isogenic lines of tomato.";
RL Theor. Appl. Genet. 96:331-338(1998).
RN [4]
RP FUNCTION.
RC STRAIN=cv. Craigella GCR237, and cv. Craigella GCR254;
RX PubMed=17238011; DOI=10.1007/s00705-006-0915-8;
RA Strasser M., Pfitzner A.J.P.;
RT "The double-resistance-breaking Tomato mosaic virus strain ToMV1-2 contains
RT two independent single resistance-breaking domains.";
RL Arch. Virol. 152:903-914(2007).
RN [5]
RP FUNCTION, MISCELLANEOUS, SUBUNIT, AND INTERACTION WITH TOBAMOVIRUSES
RP REPLICATION PROTEINS (MICROBIAL INFECTION).
RX PubMed=19423673; DOI=10.1073/pnas.0809105106;
RA Ishibashi K., Naito S., Meshi T., Ishikawa M.;
RT "An inhibitory interaction between viral and cellular proteins underlies
RT the resistance of tomato to nonadapted tobamoviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8778-8783(2009).
RN [6]
RP CRYSTALLIZATION.
RX PubMed=24316842; DOI=10.1107/s1744309113030819;
RA Kato M., Kezuka Y., Kobayashi C., Ishibashi K., Nonaka T., Ishikawa M.,
RA Katoh E.;
RT "Crystallization and preliminary X-ray crystallographic analysis of the
RT inhibitory domain of the tomato mosaic virus resistance protein Tm-1.";
RL Acta Crystallogr. F 69:1411-1414(2013).
RN [7]
RP FUNCTION.
RX PubMed=23658455; DOI=10.1128/jvi.00743-13;
RA Ishibashi K., Ishikawa M.;
RT "The resistance protein Tm-1 inhibits formation of a Tomato mosaic virus
RT replication protein-host membrane protein complex.";
RL J. Virol. 87:7933-7939(2013).
RN [8]
RP FUNCTION.
RX PubMed=23415925; DOI=10.1016/j.pep.2013.02.001;
RA Kato M., Ishibashi K., Kobayashi C., Ishikawa M., Katoh E.;
RT "Expression, purification, and functional characterization of an N-terminal
RT fragment of the tomato mosaic virus resistance protein Tm-1.";
RL Protein Expr. Purif. 89:1-6(2013).
RN [9]
RP REVIEW.
RX PubMed=25212767; DOI=10.1016/j.coviro.2014.08.005;
RA Ishibashi K., Ishikawa M.;
RT "Mechanisms of tomato mosaic virus RNA replication and its inhibition by
RT the host resistance factor Tm-1.";
RL Curr. Opin. Virol. 9:8-13(2014).
RN [10]
RP FUNCTION.
RC STRAIN=cv. Mobaci;
RX PubMed=29018314; DOI=10.5423/ppj.nt.04.2017.0082;
RA Sihelska N., Vozarova Z., Predajna L., Soltys K., Hudcovicova M.,
RA Mihalik D., Kraic J., Mrkvova M., Kudela O., Glasa M.;
RT "Experimental infection of different tomato genotypes with tomato mosaic
RT virus led to a low viral population heterogeneity in the capsid protein
RT encoding region.";
RL Plant Pathol. J. 33:508-513(2017).
RN [11]
RP FUNCTION.
RC STRAIN=cv. Mocimor;
RX PubMed=28107419; DOI=10.1371/journal.pone.0170429;
RA Luria N., Smith E., Reingold V., Bekelman I., Lapidot M., Levin I.,
RA Elad N., Tam Y., Sela N., Abu-Ras A., Ezra N., Haberman A., Yitzhak L.,
RA Lachman O., Dombrovsky A.;
RT "A new Israeli tobamovirus isolate infects tomato plants harboring Tm-2(2)
RT resistance genes.";
RL PLoS ONE 12:E0170429-E0170429(2017).
RN [12]
RP FUNCTION.
RX PubMed=29582165; DOI=10.1007/s00705-018-3819-5;
RA Maayan Y., Pandaranayaka E.P.J., Srivastava D.A., Lapidot M., Levin I.,
RA Dombrovsky A., Harel A.;
RT "Using genomic analysis to identify tomato Tm-2 resistance-breaking
RT mutations and their underlying evolutionary path in a new and emerging
RT tobamovirus.";
RL Arch. Virol. 163:1863-1875(2018).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-431 IN COMPLEX WITH ATP AND
RP TOMATO MOSAIC VIRUS REPLICATION PROTEINS, FUNCTION, SUBUNIT, AND VARIANT
RP THR-91.
RX PubMed=25092327; DOI=10.1073/pnas.1407888111;
RA Ishibashi K., Kezuka Y., Kobayashi C., Kato M., Inoue T., Nonaka T.,
RA Ishikawa M., Matsumura H., Katoh E.;
RT "Structural basis for the recognition-evasion arms race between Tomato
RT mosaic virus and the resistance gene Tm-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E3486-E3495(2014).
CC -!- FUNCTION: Inhibitor of viral RNA replication which confers resistance
CC to some tobamoviruses including tomato mosaic virus (ToMV) (e.g.
CC isolate L), tobacco mosaic virus (TMV), tobacco mild green mosaic virus
CC (TMGMV) and pepper mild mottle virus (PMMoV), but not to resistance-
CC breaking isolates of ToMV (e.g. LT1, SL-1 and ToMV1-2) and tomato brown
CC rugose fruit virus (ToBRFV) (PubMed:17699618, PubMed:3686829,
CC PubMed:17238011, PubMed:19423673, PubMed:23415925, PubMed:29582165,
CC PubMed:28107419). Prevents tobamoviruses RNA replication by affecting
CC the association of tobamoviruses replication proteins (large and small
CC subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and
CC ARL8), thus inhibiting the replication complex formation on the
CC membranes and avoiding viral negative-strand RNA synthesis
CC (PubMed:17699618, PubMed:19423673, PubMed:23658455, PubMed:23415925).
CC Inhibits triphosphatase activity of ToMV replication proteins
CC (PubMed:25092327). {ECO:0000269|PubMed:17238011,
CC ECO:0000269|PubMed:17699618, ECO:0000269|PubMed:19423673,
CC ECO:0000269|PubMed:23415925, ECO:0000269|PubMed:23658455,
CC ECO:0000269|PubMed:25092327, ECO:0000269|PubMed:28107419,
CC ECO:0000269|PubMed:29582165, ECO:0000269|PubMed:3686829}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25092327}.
CC -!- SUBUNIT: (Microbial infection) Binds, via an ATP bridge, to the
CC tobamoviruses avirulent (Avr) replication proteins (large and small
CC subunits, e.g. tomato mosaic virus (ToMV/TMV) AC P03587, tobacco mild
CC green mosaic virus (TMGMV) AC P18339 and pepper mild mottle virus
CC (PMMoV) AC P89657) to inhibit their function after the translation of
CC tobamoviruses RNA, but before the viral replication complex formation
CC on the membrane surfaces; this interaction is not possible with
CC resistance-breaking strains replication proteins.
CC {ECO:0000269|PubMed:17699618, ECO:0000269|PubMed:19423673}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to tobamoviruses
CC (ToMV,TMV). {ECO:0000269|PubMed:17699618}.
CC -!- MISCELLANEOUS: Transgenic tobacco plants expressing Tm-1 exhibit
CC resistance to tobacco mild green mosaic virus (TMGMV) and pepper mild
CC mottle virus (PMMoV), tobamoviruses that cannot multiply in tomato.
CC {ECO:0000269|PubMed:19423673}.
CC -!- MISCELLANEOUS: The Tm-1 allele present in the tomato mosaic virus
CC (ToMV/TMV)-resistant tomato cv. Craigella isolate GCR237 (AC A7M6E7)
CC confers resistance to ToMV but not the tm-1 allele present in the ToMV-
CC susceptible tomato cv. Craigella isolate GCR26 (AC A7M6E8).
CC {ECO:0000269|PubMed:17699618}.
CC -!- SIMILARITY: Belongs to the UPF0261 family. {ECO:0000305}.
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DR EMBL; AB287296; BAF75724.1; -; mRNA.
DR PDB; 3WRV; X-ray; 2.75 A; A/B=1-201.
DR PDB; 3WRW; X-ray; 2.71 A; A/B/C/D/E/F=1-431.
DR PDB; 3WRX; X-ray; 2.50 A; A/B=1-431.
DR PDB; 3WRY; X-ray; 2.30 A; A/B=1-431.
DR PDBsum; 3WRV; -.
DR PDBsum; 3WRW; -.
DR PDBsum; 3WRX; -.
DR PDBsum; 3WRY; -.
DR AlphaFoldDB; A7M6E7; -.
DR SMR; A7M6E7; -.
DR IntAct; A7M6E7; 2.
DR PRIDE; A7M6E7; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; A7M6E7; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; IDA:UniProtKB.
DR CDD; cd15488; Tm-1-like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR009215; TIM-br_IGPS-like.
DR InterPro; IPR044122; UPF0261_dom.
DR Pfam; PF09370; PEP_hydrolase; 1.
DR Pfam; PF06792; UPF0261; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Host-virus interaction; Nucleotide-binding;
KW Plant defense; Reference proteome.
FT CHAIN 1..754
FT /note="ToMV resistance protein Tm-1(GCR237)"
FT /id="PRO_0000448712"
FT REGION 1..201
FT /note="N-terminal inhibitory domain NN"
FT /evidence="ECO:0000303|PubMed:25092327"
FT REGION 211..431
FT /note="N-terminal inhibitory domain NC"
FT /evidence="ECO:0000303|PubMed:25092327"
FT BINDING 18..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25092327,
FT ECO:0007744|PDB:3WRX, ECO:0007744|PDB:3WRY"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25092327,
FT ECO:0007744|PDB:3WRX, ECO:0007744|PDB:3WRY"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25092327,
FT ECO:0007744|PDB:3WRX, ECO:0007744|PDB:3WRY"
FT BINDING 124..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25092327,
FT ECO:0007744|PDB:3WRX, ECO:0007744|PDB:3WRY"
FT VARIANT 91
FT /note="I -> T (greater ability to inhibit tomato mosaic
FT virus (ToMV/TMV) RNA replication and to bind ToMV
FT replication proteins)"
FT /evidence="ECO:0000269|PubMed:25092327"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 17..38
FT /evidence="ECO:0007829|PDB:3WRY"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 91..112
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3WRV"
FT HELIX 178..199
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3WRY"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:3WRY"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3WRY"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3WRW"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 383..397
FT /evidence="ECO:0007829|PDB:3WRY"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:3WRY"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:3WRY"
SQ SEQUENCE 754 AA; 80571 MW; DD41F56DF5B562C8 CRC64;
MATAQSNSPR VFCIGTADTK FDELRFLSEH VRSSLNSFSN KSSFKVGVTV VDVSTSWKET
NSCADFDFVP SKDVLSCHTL GEETMGTFAD IRGLAIAIMS KALETFLSIA NDEQNLAGVI
GLGGSGGTSL LSSAFRSLPI GIPKVIISTV ASGQTESYIG TSDLVLFPSV VDICGINNVS
KVVLSNAGAA FAGMVIGRLE SSKEHSITNG KFTVGVTMFG VTTPCVNAVK ERLVKEGYET
LVFHATGVGG RAMEDLVRGG FIQGVLDITT TEVADYVVGG VMACDSSRFD AILEKKIPLV
LSVGALDMVN FGPKTTIPPE FQQRKIHEHN EQVSLMRTTV GENKKFAAFI AEKLNKASSS
VCVCLPEKGV SALDAPGKDF YDPEATSCLT RELQMLLENN ERCQVKVLPY HINDAEFANA
LVDSFLEISP KSRHVECQPA ESKSIQDIQN DNAVLEKYPS CNGKNFSRLN DFPNAKPETL
QKRTVILQKL KDQISKGKPI IGAGAGTGIS AKFEEAGGVD LIVLYNSGRF RMAGRGSLAG
LLPFADANAI VLEMANEVLP VVKEVAVLAG VCATDPFRRM DNFLKQLESV GFCGVQNFPT
VGLFDGNFRQ NLEETGMGYG LEVEMIAAAH RMGLLTTPYA FCPDEAVAMA EAGADIIVAH
MGLTTSGSIG AKTAVSLEES VTCVQAIADA THRIYPDAIV LCHGGPISSP EEAAYVLKRT
TGVHGFYGAS SMERLPVEQA ITATVQQYKS ISME
